• DocumentCode
    2934912
  • Title

    Efficient method to attach enzymes to monodispersive iron nanoparticles

  • Author

    Sharma, A.M. ; Antony, J. ; Meyer, D. ; Nuttting, J. ; Paszczynski, A. ; Qiang, Y.

  • Author_Institution
    Univ. of Idaho, Moscow
  • fYear
    2006
  • fDate
    8-12 May 2006
  • Firstpage
    110
  • Lastpage
    110
  • Abstract
    One of the major concerns in environmental, biomedical and other applications of enzyme is their short life time restricting its use outside the cell. An effective way to increase the stability and longevity of enzymes from hours to days is to combine them with nanoparticles. With this aim, two different catabolic enzymes-trypsin and peroxidase were attached to the uniform magnetic iron nanoparticles. Uniform magnetic iron nanoparticles were produced from novel cluster deposition technique. The sizes of the nanoparticles deposited on petri dish were ~20 nm in diameter. The magnetic nanoparticles (MNP) were then attached to the enzymes separately and horseradish peroxide activity (HRP) was measured. The results were compared with the commercially available MNP of size diameter ~100 nm. Our study indicates that attached HRP activity of enzymeatic attached to MNP prepared in our lab was compariable and economical in comparison to commercially available nanoparticles.
  • Keywords
    biochemistry; biological techniques; biomedical materials; catalysis; catalysts; enzymes; ferromagnetic materials; iron; magnetic particles; molecular biophysics; nanobiotechnology; nanoparticles; Fe; catabolic enzymes; cluster deposition; enzyme attachment; horseradish peroxide activity; monodispersive manetic iron nanoparticles; nanoparticle size; peroxidase; trypsin; Biochemistry; Biotechnology; Iron; Laboratories; Magnetic cores; Magnetic separation; Nanoparticles; Physics; Proteins; Stability;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Magnetics Conference, 2006. INTERMAG 2006. IEEE International
  • Conference_Location
    San Diego, CA
  • Print_ISBN
    1-4244-1479-2
  • Type

    conf

  • DOI
    10.1109/INTMAG.2006.375610
  • Filename
    4261544